ID   E1BLF3_BOVIN            Unreviewed;       144 AA.
AC   E1BLF3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   14-DEC-2022, entry version 79.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU361236};
DE            EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236};
GN   Name=LOC615045 {ECO:0000313|Ensembl:ENSBTAP00000017333.5};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017333.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000017333.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000017333.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017333.5};
RG   Ensembl;
RL   Submitted (AUG-2022) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000256|ARBA:ARBA00001479};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000256|ARBA:ARBA00001479};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC         Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC         Evidence={ECO:0000256|ARBA:ARBA00001804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000256|ARBA:ARBA00001804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC         sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC         3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC         Evidence={ECO:0000256|ARBA:ARBA00001855};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000256|ARBA:ARBA00001855};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00001126};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000256|ARBA:ARBA00001126};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC         (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC         Evidence={ECO:0000256|ARBA:ARBA00001129};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC         Evidence={ECO:0000256|ARBA:ARBA00001129};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU361236};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601211-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR601211-2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU361236}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|ARBA:ARBA00007056, ECO:0000256|RuleBase:RU003654}.
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DR   RefSeq; XP_002685775.1; XM_002685729.2.
DR   RefSeq; XP_871834.1; XM_866741.3.
DR   AlphaFoldDB; E1BLF3; -.
DR   SMR; E1BLF3; -.
DR   STRING; 9913.ENSBTAP00000017333; -.
DR   PaxDb; E1BLF3; -.
DR   Ensembl; ENSBTAT00000017333.6; ENSBTAP00000017333.5; ENSBTAG00000013039.6.
DR   GeneID; 615045; -.
DR   KEGG; bta:615045; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013039; -.
DR   eggNOG; KOG4087; Eukaryota.
DR   GeneTree; ENSGT00940000155096; -.
DR   HOGENOM; CLU_090683_3_0_1; -.
DR   InParanoid; E1BLF3; -.
DR   OMA; CQCDKAA; -.
DR   OrthoDB; 1422829at2759; -.
DR   TreeFam; TF319283; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000013039; Expressed in ascending colon and 39 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601211-3};
KW   Hydrolase {ECO:0000256|RuleBase:RU361236};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361236};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601211-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361236};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT   CHAIN           24..144
FT                   /note="Phospholipase A2"
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT                   /id="PRO_5001390411"
FT   DOMAIN          21..138
FT                   /note="PA2c"
FT                   /evidence="ECO:0000259|SMART:SM00085"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   DISULFID        46..137
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        63..117
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        69..144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        70..110
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        79..103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        97..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
SQ   SEQUENCE   144 AA;  16346 MW;  37B45626AFF667F5 CRC64;
     MKTLLLLAVI MAIGLLQVHG GLADFQKMIK FTTGKEPAIS YGFYGCHCGA GHRGTPKDAT
     DWCCRVHDCC YENLRKRGCR TSSQSYNFIF QRGQIVCGDQ DYCKRRLCQC DKRAADCLDK
     NLKTYNKNLQ YYNNLLCFGS TPKC
//